ID S8A837_DACHA Unreviewed; 469 AA.
AC S8A837;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN ORFNames=H072_7073 {ECO:0000313|EMBL:EPS39180.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS39180.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS39180.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS39180.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C14B family.
CC {ECO:0000256|ARBA:ARBA00009005}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS39180.1}.
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DR EMBL; AQGS01000487; EPS39180.1; -; Genomic_DNA.
DR RefSeq; XP_011112846.1; XM_011114544.1.
DR AlphaFoldDB; S8A837; -.
DR STRING; 1284197.S8A837; -.
DR eggNOG; KOG1546; Eukaryota.
DR HOGENOM; CLU_029389_0_2_1; -.
DR OMA; ICERFRY; -.
DR OrthoDB; 1077459at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.12660; -; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR PANTHER; PTHR48104:SF30; METACASPASE-1; 1.
DR PANTHER; PTHR48104; METACASPASE-4; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022807};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 175..459
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51410 MW; A906DB9812545430 CRC64;
MSYFPGSNQG HHHQQQQQQQ QYYPPQGAPP QAGYYPPPNQ QQGYYPPPNQ YGSPPPQYPP
PQQQQYAGNY GPPSGPPPQH YPPQNQHQGY GGSYGPPAGA PPPGGSFYPP PNAQHVQHST
DNWGHTQGPR PNMPTYQSND WNRGNHHAPP PPPAGPQSFG AGLDYKWVPS KCTGRRKALL
IGINYFGQRG QLRGCINDVK NMKTFLTERY GYAIEDMVIL TDDQQNPMSM PTKANILKGM
FWLVKDARPD DSLFFHYSGH GGQQKDTDGD EDDGYDETIY PVDFRNAGMI VDDEMHKIMV
TPLQPGVRLT AIFDSCHSGS ALDLPYLYST KGVLKEPNLA KEAASGLLGA LAAYGKKDMM
GVASSLGGFL KKATTGSSAN DVSKRTKTSP ADVIQWSGSK DVQTSADTVE GGEATGAMSY
AFISALKKNP QQSYQELLNS LREELEGKYA QKPQLSCSHP LDTRTLYVM
//
